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- EMDB-24840: Human KATP channel in open conformation, focused on SUR -

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Open data


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Basic information

Entry
Database: EMDB / ID: EMD-24840
TitleHuman KATP channel in open conformation, focused on SURATP-sensitive potassium channel
Map datafocused on KATP SUR after sharpening (B-factor 82.8)
Sample
  • Complex: Human KATP channel composed of Kir6.2 (C166S G334D) and SUR1
    • Protein or peptide: ATP-binding cassette sub-family C member 8
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
Function / homology
Function and homology information


negative regulation of neuroblast migration / positive regulation of uterine smooth muscle relaxation / ATP sensitive Potassium channels / Defective ABCC8 can cause hypo- and hyper-glycemias / positive regulation of tight junction disassembly / potassium ion-transporting ATPase complex / negative regulation of blood-brain barrier permeability / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel ...negative regulation of neuroblast migration / positive regulation of uterine smooth muscle relaxation / ATP sensitive Potassium channels / Defective ABCC8 can cause hypo- and hyper-glycemias / positive regulation of tight junction disassembly / potassium ion-transporting ATPase complex / negative regulation of blood-brain barrier permeability / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel / negative regulation of low-density lipoprotein particle clearance / sulfonylurea receptor activity / positive regulation of potassium ion transport / ATPase-coupled monoatomic cation transmembrane transporter activity / response to pH / inorganic cation transmembrane transport / neuromuscular process / negative regulation of glial cell proliferation / cellular response to organic substance / response to zinc ion / potassium ion import across plasma membrane / positive regulation of insulin secretion involved in cellular response to glucose stimulus / intracellular glucose homeostasis / potassium channel activity / ATPase-coupled transmembrane transporter activity / negative regulation of insulin secretion / ABC-type transporter activity / potassium ion transmembrane transport / negative regulation of angiogenesis / Regulation of insulin secretion / female pregnancy / ADP binding / sarcolemma / response to insulin / visual learning / transmembrane transport / potassium ion transport / synaptic vesicle membrane / memory / positive regulation of tumor necrosis factor production / transmembrane transporter binding / response to lipopolysaccharide / response to xenobiotic stimulus / protein-containing complex binding / ATP hydrolysis activity / ATP binding / membrane / plasma membrane
Similarity search - Function
ATP-binding cassette subfamily C member 8 / Sulphonylurea receptor / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain ...ATP-binding cassette subfamily C member 8 / Sulphonylurea receptor / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP-binding cassette sub-family C member 8
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsZhao C / MacKinnon R
Funding support United States, 1 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2021
Title: Molecular structure of an open human K channel.
Authors: Chen Zhao / Roderick MacKinnon /
Abstract: K channels are metabolic sensors that translate intracellular ATP/ADP balance into membrane excitability. The molecular composition of K includes an inward-rectifier potassium channel (Kir) and an ...K channels are metabolic sensors that translate intracellular ATP/ADP balance into membrane excitability. The molecular composition of K includes an inward-rectifier potassium channel (Kir) and an ABC transporter-like sulfonylurea receptor (SUR). Although structures of K have been determined in many conformations, in all cases, the pore in Kir is closed. Here, we describe human pancreatic K (hK) structures with an open pore at 3.1- to 4.0-Å resolution using single-particle cryo-electron microscopy (cryo-EM). Pore opening is associated with coordinated structural changes within the ATP-binding site and the channel gate in Kir. Conformational changes in SUR are also observed, resulting in an area reduction of contact surfaces between SUR and Kir. We also observe that pancreatic hK exhibits the unique (among inward-rectifier channels) property of PIP-independent opening, which appears to be correlated with a docked cytoplasmic domain in the absence of PIP.
History
DepositionSep 12, 2021-
Header (metadata) releaseDec 1, 2021-
Map releaseDec 1, 2021-
UpdateDec 8, 2021-
Current statusDec 8, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.7
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.7
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7s5v
  • Surface level: 0.7
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_24840.png

Downloads & links

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Map

FileDownload / File: emd_24840.map.gz / Format: CCP4 / Size: 184 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationfocused on KATP SUR after sharpening (B-factor 82.8)
Voxel sizeX=Y=Z: 1.3 Å
Density
Contour LevelBy AUTHOR: 0.7 / Movie #1: 0.7
Minimum - Maximum-2.0497267 - 5.04862
Average (Standard dev.)-0.004962279 (±0.083171114)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions364364364
Spacing364364364
CellA=B=C: 473.19998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.31.31.3
M x/y/z364364364
origin x/y/z0.0000.0000.000
length x/y/z473.200473.200473.200
α/β/γ90.00090.00090.000
start NX/NY/NZ-140-140-140
NX/NY/NZ280280280
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS364364364
D min/max/mean-2.0505.049-0.005

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Supplemental data

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Sample components

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Entire : Human KATP channel composed of Kir6.2 (C166S G334D) and SUR1

EntireName: Human KATP channel composed of Kir6.2 (C166S G334D) and SUR1
Components
  • Complex: Human KATP channel composed of Kir6.2 (C166S G334D) and SUR1
    • Protein or peptide: ATP-binding cassette sub-family C member 8
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: Human KATP channel composed of Kir6.2 (C166S G334D) and SUR1

SupramoleculeName: Human KATP channel composed of Kir6.2 (C166S G334D) and SUR1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
Molecular weightTheoretical: 881.87 kDa/nm

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Macromolecule #1: ATP-binding cassette sub-family C member 8

MacromoleculeName: ATP-binding cassette sub-family C member 8 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 177.106078 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GPLAFCGSEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI HHSTWLHFPG HNLRWILTFM LLFVLVCEI AEGILSDGVT ESHHLHLYMP AGMAFMAAVT SVVYYHNIET SNFPKLLIAL LVYWTLAFIT KTIKFVKFLD H AIGFSQLR ...String:
GPLAFCGSEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI HHSTWLHFPG HNLRWILTFM LLFVLVCEI AEGILSDGVT ESHHLHLYMP AGMAFMAAVT SVVYYHNIET SNFPKLLIAL LVYWTLAFIT KTIKFVKFLD H AIGFSQLR FCLTGLLVIL YGMLLLVEVN VIRVRRYIFF KTPREVKPPE DLQDLGVRFL QPFVNLLSKG TYWWMNAFIK TA HKKPIDL RAIGKLPIAM RALTNYQRLC EAFDAQVRKD IQGTQGARAI WQALSHAFGR RLVLSSTFRI LADLLGFAGP LCI FGIVDH LGKENDVFQP KTQFLGVYFV SSQEFLANAY VLAVLLFLAL LLQRTFLQAS YYVAIETGIN LRGAIQTKIY NKIM HLSTS NLSMGEMTAG QICNLVAIDT NQLMWFFFLC PNLWAMPVQI IVGVILLYYI LGVSALIGAA VIILLAPVQY FVATK LSQA QRSTLEYSNE RLKQTNEMLR GIKLLKLYAW ENIFRTRVET TRRKEMTSLR AFAIYTSISI FMNTAIPIAA VLITFV GHV SFFKEADFSP SVAFASLSLF HILVTPLFLL SSVVRSTVKA LVSVQKLSEF LSSAEIREEQ CAPHEPTPQG PASKYQA VP LRVVNRKRPA REDCRGLTGP LQSLVPSADG DADNCCVQIM GGYFTWTPDG IPTLSNITIR IPRGQLTMIV GQVGCGKS S LLLAALGEMQ KVSGAVFWSS LPDSEIGEDP SPERETATDL DIRKRGPVAY ASQKPWLLNA TVEENIIFES PFNKQRYKM VIEACSLQPD IDILPHGDQT QIGERGINLS GGQRQRISVA RALYQHANVV FLDDPFSALD IHLSDHLMQA GILELLRDDK RTVVLVTHK LQYLPHADWI IAMKDGTIQR EGTLKDFQRS ECQLFEHWKT LMNRQDQELE KETVTERKAT EPPQGLSRAM S SRDGLLQD EEEEEEEAAE SEEDDNLSSM LHQRAEIPWR ACAKYLSSAG ILLLSLLVFS QLLKHMVLVA IDYWLAKWTD SA LTLTPAA RNCSLSQECT LDQTVYAMVF TVLCSLGIVL CLVTSVTVEW TGLKVAKRLH RSLLNRIILA PMRFFETTPL GSI LNRFSS DCNTIDQHIP STLECLSRST LLCVSALAVI SYVTPVFLVA LLPLAIVCYF IQKYFRVASR DLQQLDDTTQ LPLL SHFAE TVEGLTTIRA FRYEARFQQK LLEYTDSNNI ASLFLTAANR WLEVRMEYIG ACVVLIAAVT SISNSLHREL SAGLV GLGL TYALMVSNYL NWMVRNLADM ELQLGAVKRI HGLLKTEAES YEGLLAPSLI PKNWPDQGKI QIQNLSVRYD SSLKPV LKH VNALIAPGQK IGICGRTGSG KSSFSLAFFR MVDTFEGHII IDGIDIAKLP LHTLRSRLSI ILQDPVLFSG TIRFNLD PE RKCSDSTLWE ALEIAQLKLV VKALPGGLDA IITEGGENFS QGQRQLFCLA RAFVRKTSIF IMDEATASID MATENILQ K VVMTAFADRT VVTIAHRVHT ILSADLVIVL KRGAILEFDK PEKLLSRKDS VFASFVRADK

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Macromolecule #2: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration6.83 mg/mL
BufferpH: 8.5
GridModel: Quantifoil R1.2/1.3 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 289 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 57.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 144706
FSC plot (resolution estimation)

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